PATA_HELPY
ID PATA_HELPY Reviewed; 527 AA.
AC O25526;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Peptidoglycan O-acetyltransferase;
DE Short=PG acetyltransferase;
DE EC=2.3.1.-;
GN Name=patA; OrderedLocusNames=HP_0855, C694_04380;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RA Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA Kostrjukova E., Govorun V.;
RT "Draft genome of Helicobacter pylori.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN PG O-ACETYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700392 / 26695, and X47;
RX PubMed=23221800; DOI=10.1128/mbio.00409-12;
RA Wang G., Lo L.F., Forsberg L.S., Maier R.J.;
RT "Helicobacter pylori peptidoglycan modifications confer lysozyme resistance
RT and contribute to survival in the host.";
RL MBio 3:E00409-E00412(2012).
CC -!- FUNCTION: Catalyzes the O-acetylation of peptidoglycan (PG), an
CC important mechanism that appears to confer lysozyme resistance and
CC contributes to pathogen persistence in the host.
CC {ECO:0000269|PubMed:23221800}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene contain a greatly reduced
CC amount of acetylated muropeptides in the bacterial PG, and are more
CC susceptible to lysozyme killing than wild-type.
CC {ECO:0000269|PubMed:23221800}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07902.1; -; Genomic_DNA.
DR EMBL; CP003904; AFV42066.1; -; Genomic_DNA.
DR PIR; G64626; G64626.
DR RefSeq; NP_207649.1; NC_000915.1.
DR RefSeq; WP_000881300.1; NC_018939.1.
DR AlphaFoldDB; O25526; -.
DR SMR; O25526; -.
DR STRING; 85962.C694_04380; -.
DR PaxDb; O25526; -.
DR EnsemblBacteria; AAD07902; AAD07902; HP_0855.
DR KEGG; heo:C694_04380; -.
DR KEGG; hpy:HP_0855; -.
DR PATRIC; fig|85962.47.peg.909; -.
DR eggNOG; COG1696; Bacteria.
DR HOGENOM; CLU_025255_1_3_7; -.
DR OMA; IIWGAWH; -.
DR PhylomeDB; O25526; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR028362; AlgI.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF500217; AlgI; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..527
FT /note="Peptidoglycan O-acetyltransferase"
FT /id="PRO_0000424441"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 363
FT /evidence="ECO:0000255"
SQ SEQUENCE 527 AA; 61245 MW; F90AE76E8CE9B3BB CRC64;
MLASIISILR VFVLLFNTPL FIFAFLPVGF LGYFILQAYA KNPLFPKLWL VLASLFFYAF
WNVKYLPLLV GSIVFNYFVA LKIHQTQPNA YKRLWLILGL IANVSLLGFF KYTDFFLTNF
NLIWKSHFET LHLILPLAIS FFTLQQIAYL MDTYKQNQIM QPKMRERVSE NAPILLNPPT
SFFSLSHFLD YALFVSFFPQ LIAGPIVHHS EMMPQFKDKN NQYLNYRNIA LGLFIFSIGL
FKKVVIADNT AHFADFGFDK ATSLSFIQAW MTSLSYSFQL YFDFSGYCDM AIGIGLFFNI
KLPINFNSPY KALNIQDFWR RWHITLSRFL KEYLYIPLGG NRVKELIVYR NLILVFLIGG
FWHGAGWTFI IWGLLHGIAL SVHRAYSHAT RKFHFTMPKI LAWLITFNFI NLAWVFFRAK
NLESALKVLK GMVGLNGVSL CHLSKEASEF LNRVNDNMIM HTIMYASPTF KMCVLMIIIS
FCLKNSSHLY QSNQMDWIKT TSACLLLSIG FLFIFASSQS VFLYFNF
